2ctn

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(New page: 200px<br /><applet load="2ctn" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ctn" /> '''STRUCTURE OF CALCIUM-SATURATED CARDIAC TROPO...)
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[[Image:2ctn.jpg|left|200px]]<br /><applet load="2ctn" size="350" color="white" frame="true" align="right" spinBox="true"
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'''STRUCTURE OF CALCIUM-SATURATED CARDIAC TROPONIN C, NMR, 30 STRUCTURES'''<br />
'''STRUCTURE OF CALCIUM-SATURATED CARDIAC TROPONIN C, NMR, 30 STRUCTURES'''<br />
==Overview==
==Overview==
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The regulation of cardiac muscle contraction must differ from that of, skeletal muscles to effect different physiological and contractile, properties. Cardiac troponin C (TnC), the key regulator of cardiac muscle, contraction, possesses different functional and Ca2+-binding properties, compared with skeletal TnC and features a Ca2+-binding site I, which is, naturally inactive. The structure of cardiac TnC in the Ca2+-saturated, state has been determined by nuclear magnetic resonance spectroscopy. The, regulatory domain exists in a "closed" conformation even in the Ca2+-bound, (the "on") state, in contrast to all predicted models and differing, significantly from the calcium-induced structure observed in skeletal TnC., This structure in the Ca2+-bound state, and its subsequent interaction, with troponin I (TnI), are crucial in determining the specific regulatory, mechanism for cardiac muscle contraction. Further, it will allow for an, understanding of the action of calcium-sensitizing drugs, which bind to, cardiac TnC and are known to enhance the ability of cardiac TnC to, activate cardiac muscle contraction.
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The regulation of cardiac muscle contraction must differ from that of skeletal muscles to effect different physiological and contractile properties. Cardiac troponin C (TnC), the key regulator of cardiac muscle contraction, possesses different functional and Ca2+-binding properties compared with skeletal TnC and features a Ca2+-binding site I, which is naturally inactive. The structure of cardiac TnC in the Ca2+-saturated state has been determined by nuclear magnetic resonance spectroscopy. The regulatory domain exists in a "closed" conformation even in the Ca2+-bound (the "on") state, in contrast to all predicted models and differing significantly from the calcium-induced structure observed in skeletal TnC. This structure in the Ca2+-bound state, and its subsequent interaction with troponin I (TnI), are crucial in determining the specific regulatory mechanism for cardiac muscle contraction. Further, it will allow for an understanding of the action of calcium-sensitizing drugs, which bind to cardiac TnC and are known to enhance the ability of cardiac TnC to activate cardiac muscle contraction.
==About this Structure==
==About this Structure==
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2CTN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CTN OCA].
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2CTN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CTN OCA].
==Reference==
==Reference==
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Gagne, S.M.]]
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[[Category: Gagne, S M.]]
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[[Category: Li, M.X.]]
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[[Category: Li, M X.]]
[[Category: Liu, W.]]
[[Category: Liu, W.]]
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[[Category: Putkey, J.A.]]
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[[Category: Putkey, J A.]]
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[[Category: Sia, S.K.]]
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[[Category: Sia, S K.]]
[[Category: Spyracopoulos, L.]]
[[Category: Spyracopoulos, L.]]
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[[Category: Sykes, B.D.]]
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[[Category: Sykes, B D.]]
[[Category: CA]]
[[Category: CA]]
[[Category: calcium-binding protein]]
[[Category: calcium-binding protein]]
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[[Category: regulatory]]
[[Category: regulatory]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:15:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:52:28 2008''

Revision as of 14:52, 21 February 2008


2ctn

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STRUCTURE OF CALCIUM-SATURATED CARDIAC TROPONIN C, NMR, 30 STRUCTURES

Overview

The regulation of cardiac muscle contraction must differ from that of skeletal muscles to effect different physiological and contractile properties. Cardiac troponin C (TnC), the key regulator of cardiac muscle contraction, possesses different functional and Ca2+-binding properties compared with skeletal TnC and features a Ca2+-binding site I, which is naturally inactive. The structure of cardiac TnC in the Ca2+-saturated state has been determined by nuclear magnetic resonance spectroscopy. The regulatory domain exists in a "closed" conformation even in the Ca2+-bound (the "on") state, in contrast to all predicted models and differing significantly from the calcium-induced structure observed in skeletal TnC. This structure in the Ca2+-bound state, and its subsequent interaction with troponin I (TnI), are crucial in determining the specific regulatory mechanism for cardiac muscle contraction. Further, it will allow for an understanding of the action of calcium-sensitizing drugs, which bind to cardiac TnC and are known to enhance the ability of cardiac TnC to activate cardiac muscle contraction.

About this Structure

2CTN is a Single protein structure of sequence from Gallus gallus with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of cardiac muscle troponin C unexpectedly reveals a closed regulatory domain., Sia SK, Li MX, Spyracopoulos L, Gagne SM, Liu W, Putkey JA, Sykes BD, J Biol Chem. 1997 Jul 18;272(29):18216-21. PMID:9218458

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